ID A4CPH1_ROBBH Unreviewed; 367 AA.
AC A4CPH1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Linoleoyl-CoA desaturase {ECO:0000313|EMBL:EAR14292.1};
GN OrderedLocusNames=RB2501_02670 {ECO:0000313|EMBL:EAR14292.1};
OS Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Robiginitalea.
OX NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR14292.1, ECO:0000313|Proteomes:UP000009049};
RN [1] {ECO:0000313|EMBL:EAR14292.1, ECO:0000313|Proteomes:UP000009049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC {ECO:0000313|Proteomes:UP000009049};
RX PubMed=19767438; DOI=10.1128/JB.01191-09;
RA Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL J. Bacteriol. 191:7144-7145(2009).
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295}.
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DR EMBL; CP001712; EAR14292.1; -; Genomic_DNA.
DR RefSeq; WP_015755728.1; NC_013222.1.
DR AlphaFoldDB; A4CPH1; -.
DR STRING; 313596.RB2501_02670; -.
DR KEGG; rbi:RB2501_02670; -.
DR eggNOG; COG3239; Bacteria.
DR HOGENOM; CLU_030320_0_0_10; -.
DR OrthoDB; 104711at2; -.
DR Proteomes; UP000009049; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProt.
DR CDD; cd03506; Delta6-FADS-like; 1.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353:SF19; DELTA(5) FATTY ACID DESATURASE C-RELATED; 1.
DR PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009049};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..341
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 367 AA; 43095 MW; F1DB70725A9A502C CRC64;
MSENAIRFSR TESPQFFRTL NKRVNAYFKE NGLKKTGNWQ LYLKTAVMFS LLLAPYFLIL
TLGLPTWANL LLTMLMGVGM AGVGMNVMHD GNHGTYSSRK WINKLMGGSI YLLAGNVYNW
QVQHNVLHHT YTNIHEHDED LEAGRILRFS KHAKWHRFHR FQHYYSVFLY GLLTFNWAIT
TDFQQMYRYT KRKLAYGKFP NPVLNWSVLV ITKLIYLFIW IALPIIIMDI AWWKVVLGFF
IMHYVAGVIL SVVFQLAHVV DHADMPLPEK DGTMKNSWAI HQLRTTVNFG TRNRIVNWFT
GGLNHQVEHH IFPNISHVHY TKISKIVKQT AREFNLPYNE YKTTRKAIIS HFRHLRELGK
KPSLQLQ
//
